Article
New conformational properties induced by the replacement of Tyr-64 in Desulfovibrio vulgaris Hildenborough ferricytochrome c553 using isotopic exchanges monitored by mass spectrometry.
FEBS letters - 14 Oct 1996
Guy P, Jaquinod M, Rémigy H, Andrieu J P, Gagnon J, Bersch B, Dolla A, Blanchard L, Guerlesquin F, Forest E
Abstract excerpt
In order to study the conformational stability induced by the replacement of Tyr-64 in Desulfovibrio vulgaris Hildenborough (DvH) cytochrome c553, fast peptic digestion of deuterated protein followed by separation and measurement of related peptides using liquid chromatography coupled to electrospray ionization mass spectrometry was performed. We show that the H-bonding and/or solvent accessibility properties...
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